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Protein

Proteasome subunit alpha type-1

Gene

SCL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.

Miscellaneous

Present with 15200 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • proteasomal ubiquitin-independent protein catabolic process Source: SGD
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciYEAST:G3O-30533-MONOMER
ReactomeiR-SCE-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-SCE-174113 SCF-beta-TrCP mediated degradation of Emi1
R-SCE-187577 SCF(Skp2)-mediated degradation of p27/p21
R-SCE-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-SCE-382556 ABC-family proteins mediated transport
R-SCE-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-SCE-5668541 TNFR2 non-canonical NF-kB pathway
R-SCE-5687128 MAPK6/MAPK4 signaling
R-SCE-5689880 Ub-specific processing proteases
R-SCE-68949 Orc1 removal from chromatin
R-SCE-69017 CDK-mediated phosphorylation and removal of Cdc6
R-SCE-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-SCE-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-SCE-983168 Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MEROPSiT01.971

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-1 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C7-alpha
Multicatalytic endopeptidase complex C7
Proteasome component C7-alpha
Proteasome component Y8
Proteinase YSCE subunit 7
SCL1 suppressor protein
Gene namesi
Name:SCL1
Synonyms:PRC2, PRS2
Ordered Locus Names:YGL011C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi

Organism-specific databases

EuPathDBiFungiDB:YGL011C
SGDiS000002979 SCL1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001241412 – 252Proteasome subunit alpha type-1Add BLAST251

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Cross-linki232Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei237PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP21243
PaxDbiP21243
PRIDEiP21243

2D gel databases

UCD-2DPAGEiP21243

PTM databases

iPTMnetiP21243

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with CIC1.2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi33235, 381 interactors
DIPiDIP-2810N
IntActiP21243, 30 interactors
MINTiP21243
STRINGi4932.YGL011C

Structurei

Secondary structure

1252
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 14Combined sources4
Beta strandi16 – 18Combined sources3
Turni21 – 23Combined sources3
Helixi26 – 34Combined sources9
Turni35 – 38Combined sources4
Beta strandi42 – 46Combined sources5
Beta strandi48 – 56Combined sources9
Beta strandi62 – 64Combined sources3
Helixi66 – 68Combined sources3
Beta strandi71 – 74Combined sources4
Beta strandi76 – 78Combined sources3
Beta strandi80 – 85Combined sources6
Helixi87 – 108Combined sources22
Helixi114 – 130Combined sources17
Beta strandi131 – 134Combined sources4
Beta strandi140 – 147Combined sources8
Turni148 – 150Combined sources3
Beta strandi151 – 157Combined sources7
Turni159 – 161Combined sources3
Beta strandi163 – 172Combined sources10
Helixi175 – 189Combined sources15
Beta strandi191 – 193Combined sources3
Helixi199 – 214Combined sources16
Beta strandi222 – 229Combined sources8
Beta strandi232 – 235Combined sources4
Helixi238 – 248Combined sources11
Turni249 – 251Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20A/O1-252[»]
1G0UX-ray2.40G/U1-252[»]
1G65X-ray2.25G/U10-252[»]
1JD2X-ray3.002/G10-252[»]
1RYPX-ray1.90A/O10-252[»]
1Z7QX-ray3.22A/O1-252[»]
2F16X-ray2.80G/U10-252[»]
2FAKX-ray2.80G/U10-252[»]
2GPLX-ray2.81G/U10-252[»]
2ZCYX-ray2.90G/U1-252[»]
3BDMX-ray2.70G/U1-252[»]
3D29X-ray2.60G/U12-252[»]
3DY3X-ray2.81G/U10-252[»]
3DY4X-ray2.80G/U10-252[»]
3E47X-ray3.00G/U10-252[»]
3GPJX-ray2.70G/U10-252[»]
3GPTX-ray2.41G/U10-252[»]
3GPWX-ray2.50G/U10-252[»]
3HYEX-ray2.50G/U10-252[»]
3JCOelectron microscopy4.80A/a1-252[»]
3JCPelectron microscopy4.60A/a1-252[»]
3MG0X-ray2.68G/U10-252[»]
3MG4X-ray3.11G/U10-252[»]
3MG6X-ray2.60G/U1-252[»]
3MG7X-ray2.78G/U1-252[»]
3MG8X-ray2.59G/U1-252[»]
3NZJX-ray2.40G/U1-252[»]
3NZWX-ray2.50G/U1-252[»]
3NZXX-ray2.70G/U1-252[»]
3OEUX-ray2.60G/U10-252[»]
3OEVX-ray2.85G/U10-252[»]
3OKJX-ray2.70G/U10-252[»]
3SDIX-ray2.65G/U10-252[»]
3SDKX-ray2.70G/U10-252[»]
3SHJX-ray2.80G/U10-252[»]
3TDDX-ray2.70G/U10-252[»]
3UN4X-ray3.40G/U1-252[»]
3UN8X-ray2.70G/U1-252[»]
3WXRX-ray3.15A/O1-252[»]
4CR2electron microscopy7.70A1-252[»]
4CR3electron microscopy9.30A1-252[»]
4CR4electron microscopy8.80A1-252[»]
4EU2X-ray2.51A/O10-250[»]
4FZCX-ray2.80G/U10-252[»]
4FZGX-ray3.00G/U10-252[»]
4G4SX-ray2.49A1-252[»]
4GK7X-ray2.80G/U10-252[»]
4HNPX-ray2.80G/U10-252[»]
4HRCX-ray2.80G/U10-252[»]
4HRDX-ray2.80G/U10-252[»]
4INRX-ray2.70G/U1-252[»]
4INTX-ray2.90G/U1-252[»]
4INUX-ray3.10G/U1-252[»]
4J70X-ray2.80G/U1-252[»]
4JSQX-ray2.80G/U1-252[»]
4JSUX-ray2.90G/U1-252[»]
4JT0X-ray3.10G/U1-252[»]
4LQIX-ray2.70G/U10-252[»]
4LTCX-ray2.50G/U1-252[»]
4NNNX-ray2.50G/U1-252[»]
4NNWX-ray2.60G/U1-252[»]
4NO1X-ray2.50G/U1-252[»]
4NO6X-ray3.00G/U1-252[»]
4NO8X-ray2.70G/U1-252[»]
4NO9X-ray2.90G/U1-252[»]
4Q1SX-ray2.60G/U1-252[»]
4QBYX-ray3.00G/U1-252[»]
4QLQX-ray2.40G/U1-252[»]
4QLSX-ray2.80G/U1-252[»]
4QLTX-ray2.80G/U1-252[»]
4QLUX-ray2.80G/U1-252[»]
4QLVX-ray2.90G/U1-252[»]
4QUXX-ray3.00G/U1-252[»]
4QUYX-ray2.80G/U1-252[»]
4QV0X-ray3.10G/U1-252[»]
4QV1X-ray2.50G/U1-252[»]
4QV3X-ray3.00G/U1-252[»]
4QV4X-ray2.70G/U1-252[»]
4QV5X-ray2.70G/U1-252[»]
4QV6X-ray2.80G/U1-252[»]
4QV7X-ray2.60G/U1-252[»]
4QV8X-ray2.90G/U1-252[»]
4QV9X-ray2.60G/U1-252[»]
4QVLX-ray2.80G/U1-252[»]
4QVMX-ray2.80G/U1-252[»]
4QVNX-ray2.90G/U1-252[»]
4QVPX-ray2.30G/U1-252[»]
4QVQX-ray2.60G/U1-252[»]
4QVVX-ray2.80G/U1-252[»]
4QVWX-ray3.00G/U1-252[»]
4QVYX-ray2.51G/U1-252[»]
4QW0X-ray2.90G/U1-252[»]
4QW1X-ray2.90G/U1-252[»]
4QW3X-ray2.90G/U1-252[»]
4QW4X-ray2.80G/U1-252[»]
4QW5X-ray3.00G/U1-252[»]
4QW6X-ray2.90G/U1-252[»]
4QW7X-ray2.70G/U1-252[»]
4QWFX-ray3.00G/U1-252[»]
4QWGX-ray2.60G/U1-252[»]
4QWIX-ray2.60G/U1-252[»]
4QWJX-ray2.90G/U1-252[»]
4QWKX-ray2.80G/U1-252[»]
4QWLX-ray2.60G/U1-252[»]
4QWRX-ray2.90G/U1-252[»]
4QWSX-ray3.00G/U1-252[»]
4QWUX-ray3.00G/U1-252[»]
4QWXX-ray2.90G/U1-252[»]
4QXJX-ray2.80G/U1-252[»]
4QZ0X-ray3.00G/U1-252[»]
4QZ1X-ray3.00G/U1-252[»]
4QZ2X-ray2.70G/U1-252[»]
4QZ3X-ray2.80G/U1-252[»]
4QZ4X-ray3.00G/U1-252[»]
4QZ5X-ray2.80G/U1-252[»]
4QZ6X-ray2.90G/U1-252[»]
4QZ7X-ray2.80G/U1-252[»]
4QZWX-ray3.00G/U1-252[»]
4QZXX-ray2.60G/U1-252[»]
4QZZX-ray2.90G/U1-252[»]
4R00X-ray2.80G/U1-252[»]
4R02X-ray2.50G/U1-252[»]
4R17X-ray2.10G/U1-252[»]
4R18X-ray2.40G/U1-252[»]
4RURX-ray2.50G/U1-252[»]
4V7OX-ray3.00AA/AC/BA/BO10-252[»]
4X6ZX-ray2.70A/O1-252[»]
4Y69X-ray2.90G/U1-252[»]
4Y6AX-ray2.60G/U1-252[»]
4Y6VX-ray2.80G/U1-252[»]
4Y6ZX-ray2.70G/U1-252[»]
4Y70X-ray2.40G/U1-252[»]
4Y74X-ray2.70G/U1-252[»]
4Y75X-ray2.80G/U1-252[»]
4Y77X-ray2.50G/U1-252[»]
4Y78X-ray2.80G/U1-252[»]
4Y7WX-ray2.50G/U1-252[»]
4Y7XX-ray2.60G/U1-252[»]
4Y7YX-ray2.40G/U1-252[»]
4Y80X-ray2.50G/U1-252[»]
4Y81X-ray2.80G/U1-252[»]
4Y82X-ray2.80G/U1-252[»]
4Y84X-ray2.70G/U1-252[»]
4Y8GX-ray2.60G/U1-252[»]
4Y8HX-ray2.50G/U1-252[»]
4Y8IX-ray2.60G/U1-252[»]
4Y8JX-ray2.70G/U1-252[»]
4Y8KX-ray2.60G/U1-252[»]
4Y8LX-ray2.40G/U1-252[»]
4Y8MX-ray2.80G/U1-252[»]
4Y8NX-ray2.60G/U1-252[»]
4Y8OX-ray2.70G/U1-252[»]
4Y8PX-ray2.80G/U1-252[»]
4Y8QX-ray2.60G/U1-252[»]
4Y8RX-ray2.70G/U1-252[»]
4Y8SX-ray2.70G/U1-252[»]
4Y8TX-ray2.70G/U1-252[»]
4Y8UX-ray2.90G/U1-252[»]
4Y9YX-ray2.80G/U1-252[»]
4Y9ZX-ray2.80G/U1-252[»]
4YA0X-ray2.80G/U1-252[»]
4YA1X-ray2.90G/U1-252[»]
4YA2X-ray2.70G/U1-252[»]
4YA3X-ray2.70G/U1-252[»]
4YA4X-ray2.90G/U1-252[»]
4YA5X-ray2.50G/U1-252[»]
4YA7X-ray2.70G/U1-252[»]
4YA9X-ray2.70G/U1-252[»]
4Z1LX-ray3.00G/U1-252[»]
5A5Belectron microscopy9.50A1-252[»]
5AHJX-ray2.80G/U1-252[»]
5BOUX-ray2.60G/U1-252[»]
5BXLX-ray2.80G/U1-252[»]
5BXNX-ray2.80G/U1-252[»]
5CGFX-ray2.80G/U1-252[»]
5CGGX-ray2.90G/U1-252[»]
5CGHX-ray2.50G/U1-252[»]
5CGIX-ray2.80G/U1-252[»]
5CZ4X-ray2.30G/U1-252[»]
5CZ5X-ray2.80G/U1-252[»]
5CZ6X-ray2.70G/U1-252[»]
5CZ7X-ray2.50G/U1-252[»]
5CZ8X-ray2.80G/U1-252[»]
5CZ9X-ray2.90G/U1-252[»]
5CZAX-ray2.50G/U1-252[»]
5D0SX-ray2.50G/U1-252[»]
5D0TX-ray2.60G/U1-252[»]
5D0VX-ray2.90G/U1-252[»]
5D0WX-ray2.80G/U1-252[»]
5D0XX-ray2.60G/U1-252[»]
5D0ZX-ray2.90G/U1-252[»]
5DKIX-ray2.80G/U1-252[»]
5DKJX-ray2.80G/U1-252[»]
5FG7X-ray2.70G/U1-252[»]
5FG9X-ray2.60G/U1-252[»]
5FGAX-ray2.70G/U1-252[»]
5FGDX-ray2.80G/U1-252[»]
5FGEX-ray2.60G/U1-252[»]
5FGFX-ray2.60G/U1-252[»]
5FGGX-ray2.70G/U1-252[»]
5FGHX-ray2.80G/U1-252[»]
5FGIX-ray2.90G/U1-252[»]
5FHSX-ray2.70G/U1-252[»]
5JHRX-ray2.90G/U1-252[»]
5JHSX-ray3.00G/U1-252[»]
5L52X-ray2.70G/U1-252[»]
5L54X-ray2.80G/U1-252[»]
5L55X-ray2.90G/U1-252[»]
5L5AX-ray2.40G/U1-252[»]
5L5BX-ray2.80G/U1-252[»]
5L5DX-ray2.80G/U1-252[»]
5L5EX-ray2.90G/U1-252[»]
5L5FX-ray2.50G/U1-252[»]
5L5HX-ray2.60G/U1-252[»]
5L5IX-ray2.90G/U1-252[»]
5L5JX-ray2.90G/U1-252[»]
5L5OX-ray2.60G/U1-252[»]
5L5PX-ray2.80G/U1-252[»]
5L5QX-ray2.80G/U1-252[»]
5L5RX-ray2.90G/U1-252[»]
5L5SX-ray2.60G/U1-252[»]
5L5TX-ray2.90G/U1-252[»]
5L5UX-ray2.60G/U1-252[»]
5L5VX-ray2.70G/U1-252[»]
5L5WX-ray2.80G/U1-252[»]
5L5XX-ray2.90G/U1-252[»]
5L5YX-ray2.70G/U1-252[»]
5L5ZX-ray2.70G/U1-252[»]
5L60X-ray2.70G/U1-252[»]
5L61X-ray2.80G/U1-252[»]
5L62X-ray2.80G/U1-252[»]
5L63X-ray2.70G/U1-252[»]
5L64X-ray2.70G/U1-252[»]
5L65X-ray2.90G/U1-252[»]
5L66X-ray2.80G/U1-252[»]
5L67X-ray2.60G/U1-252[»]
5L68X-ray2.80G/U1-252[»]
5L69X-ray2.70G/U1-252[»]
5L6AX-ray2.80G/U1-252[»]
5L6BX-ray2.60G/U1-252[»]
5L6CX-ray2.60G/U1-252[»]
5LAIX-ray2.50G/U1-252[»]
5LAJX-ray2.90G/U1-252[»]
5LTTX-ray2.70G/U1-252[»]
5M2BX-ray2.70G/U1-252[»]
5MP9electron microscopy4.10A/a1-252[»]
5MPAelectron microscopy4.50A/a1-252[»]
5MPBelectron microscopy7.80A/a1-252[»]
5MPCelectron microscopy7.70A/a1-252[»]
5NIFX-ray3.00A/O1-252[»]
5WVIelectron microscopy6.30A/c1-252[»]
5WVKelectron microscopy4.20A/c1-252[»]
ProteinModelPortaliP21243
SMRiP21243
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21243

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074807
HOGENOMiHOG000091084
InParanoidiP21243
KOiK02730
OMAiYGYEITP
OrthoDBiEOG092C47D8

Family and domain databases

CDDicd03754 proteasome_alpha_type_6, 1 hit
Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
IPR034642 Proteasome_subunit_alpha6
PANTHERiPTHR11599:SF11 PTHR11599:SF11, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PF10584 Proteasome_A_N, 1 hit
SMARTiView protein in SMART
SM00948 Proteasome_A_N, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00388 PROTEASOME_ALPHA_1, 1 hit
PS51475 PROTEASOME_ALPHA_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21243-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGAAAASAA GYDRHITIFS PEGRLYQVEY AFKATNQTNI NSLAVRGKDC
60 70 80 90 100
TVVISQKKVP DKLLDPTTVS YIFCISRTIG MVVNGPIPDA RNAALRAKAE
110 120 130 140 150
AAEFRYKYGY DMPCDVLAKR MANLSQIYTQ RAYMRPLGVI LTFVSVDEEL
160 170 180 190 200
GPSIYKTDPA GYYVGYKATA TGPKQQEITT NLENHFKKSK IDHINEESWE
210 220 230 240 250
KVVEFAITHM IDALGTEFSK NDLEVGVATK DKFFTLSAEN IEERLVAIAE

QD
Length:252
Mass (Da):28,001
Last modified:May 1, 1991 - v1
Checksum:i5B938C862BC8D7EB
GO

Sequence cautioni

The sequence AAA35020 differs from that shown. Reason: Frameshift at position 26.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31430 Genomic DNA Translation: AAA35020.1 Frameshift.
X56971 Genomic DNA Translation: CAA40292.1
M55440 mRNA Translation: AAA35228.1
M63641 Genomic DNA Translation: AAA34909.1
X56732 Genomic DNA Translation: CAA40056.1
S58126 Genomic DNA Translation: AAD13894.1
Z72533 Genomic DNA Translation: CAA96711.1
BK006941 Genomic DNA Translation: DAA08087.1
PIRiS11199 SNBYS1
RefSeqiNP_011504.3, NM_001180876.3

Genome annotation databases

EnsemblFungiiYGL011C; YGL011C; YGL011C
GeneIDi852873
KEGGisce:YGL011C

Entry informationi

Entry nameiPSA1_YEAST
AccessioniPrimary (citable) accession number: P21243
Secondary accession number(s): D6VUC6, P15708
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: May 23, 2018
This is version 207 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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